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Glycobiology Advance Access published online on September 23, 2007
Glycobiology, doi:10.1093/glycob/cwm103
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© The Author 2007. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Molecular Cloning Of Squid N-Acetylgalactosamine 4-Sulfate 6-O-Sulfotransferase And Synthesis Of a Unique Chondroitin Sulfate Containing E-D Hybrid Tetrasaccharide Structure By The Recombinant Enzyme

Teruyoshi Tamaguchi1, Shiori Ohtake1,2,, Koji Kimata2 and Osami Habuchi1,3

1 Department of Chemistry, Aichi University of Education, Igaya-cho, Kariya, Aichi 448–8542, Japan
2 Institute for Molecular Science of Medicine, Aichi Medical University, Nagakute, Aichi 480–1195, Japan

Address correspondence to: Dr. Osami Habuchi, Department of Chemistry, Aichi University of Education Igaya-cho, Kariya, Aichi 448-8542, Japan, FAX: 81-566-26-2649, E-mail: ohabuchi{at}auecc.aichi-edu.ac.jp

Received on June 9, 2007; accepted on September 20, 2007

N-Acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) transfers sulfate to position 6 of GalNAc(4SO4) residues in chondroitin sulfate (CS). We previously purified squid GalNAc4S-6ST and cloned a cDNA encoding partial sequence of squid GalNAc4S-6ST. In this paper, we cloned squid GalNAc4S-6ST cDNA containing a full open reading frame and characterized the recombinant squid GalNAc4S-6ST. The cDNA predicts a Type II transmembrane protein composed of 425 amino acid residues. The recombinant squid GalNAc4S-6ST transferred sulfate preferentially to the internal GalNAc(4SO4) residues of CS-A; nevertheless, the nonreducing terminal GalNAc(4SO4) could be sulfated efficiently when the GalNAc(4SO4) residue was included in the unique nonreducing terminal structure, GalNAc(4SO4)-GlcA(2SO4)-GalNAc(6SO4), which was previously found in CS-A. Shark cartilage CS-C and CS-D, poor acceptors for human GalNAc4S-6ST, served as the good acceptors for the recombinant squid GalNAc4S-6ST. Analysis of the sulfated products formed from CS-C and CS-D revealed that GalNAc(4SO4) residues included in a tetrasaccharide sequence, GlcA-GalNAc(4SO4)-GlcA(2SO4)-GalNAc(6SO4), was sulfated efficiently by squid GalNAc4S-6ST, and the E-D hybrid tetrasaccharide sequence, GlcA-GalNAc(4,6-SO4)-GlcA(2SO4)-GalNAc(6SO4) was generated in the resulting sulfated glycosaminoglycans. These observations indicate that the recombinant squid GalNAc4S-6ST is a useful enzyme for preparing a unique chondroitin sulfate containing the E-D hybrid tetrasaccharide structure.

Key words: GalNAc4S-6ST / squid / sulfotransferase / chondroitin sulfate E / chondroitin sulfate D


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